To gain insight into the physicochemical characteristics and molecular structure of G protein-coupled estrogen receptor 1 (GPER1), series of bioinformatics tools were used to analyze human GPRE1, its physical-chemical properties, signal peptide region, transmembrane domains, subcellular localization, phosphorylation sites and glycosylated sites, secondary structure, conserve domain, protein-protein interaction networks and correlation with tumor. GPER1 has a relative molecular weight of 42 247.59 Da, its theoretical isoelectric point is 8.63, molecular formula is C1938H3018N510O509S20, unstable coefficient is 48.12, adipose coefficient is 110.51, the average of hydrophilicity is 0.449. GPER1 is a hydrophobic and unstable protein, with 7 transmembrane domains, localized in the plasma membrane (60.9%), endoplasmic reticulum (13.0%) and vacuolar (17.4%), respectively. The secondary structure mainly involves alpha-helix, 4 N-glycosylation sites and 10 O-glycosylation, 27 phosphorylation sites. The interacting proteins of GPER1 mainly include 10 proteins such as ESR1, DLG4, GNAQ and so on. In addition, GPER1 was lowly expressed in UCEC (uterine corpus endometrial carcinoma) tissues, and GPER1 gene mutation group suggesting that the overall survival of UCEC patients significantly decreased. Human GPER1 could be a key factor in the GPCRs (G protein-coupled receptors) signaling pathway, which provided an important reference for further exploring its roles in the molecular mechanism of tumor.